Cloned (Comment) | Organism |
---|---|
DNA and amino acid sequence determination and analysis, sequence comparisons, functional recombinant expression in Saccharomyces cerevisiae and CHO-S cells, expression in Escherichia coli strains is not successful | Crassostrea virginica |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Crassostrea virginica | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Crassostrea virginica | the recombinant alpha-Kdo-ase effectively hydrolyzes the alpha-ketoside in the core-oligosaccharide of the structurally defined lipopolysaccharide (LPS), Re-LPS (Kdo2-lipid A) from Salmonella minnesota strain R595 and Escherichia coli strain D31m4, while Rd-LPS from Salmonella minnesota strain R7, that contains an extra outer core phosphorylated heptose, is only slowly hydrolyzed. The complex type LPS from Neisseria meningitides strains A1 and M992 that contain extra 5-6 sugar units at the outer core are refractory to recombinnat alpha-Kdo-ase | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Crassostrea virginica | A0A0M3N009 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant extracellular enzyme from Pichia pastoris and Saccharomyces cerevisiae in large scale by ultracentrifugation of culture supernatant, followed by two steps ultrafiltration and gel filtration, recombinnat His-tagged enzyme from Pichia pastoris by nickel affinity chromatography and gel filtration | Crassostrea virginica |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
hepatopancreas | - |
Crassostrea virginica | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-methylumbelliferyl 3-deoxy-alpha-D-manno-oct-2-ulosonic acid + H2O | - |
Crassostrea virginica | 4-methylumbelliferone + 3-deoxy-D-manno-oct-2-ulosonic acid | - |
? | |
additional information | the recombinant alpha-Kdo-ase effectively hydrolyzes the alpha-ketoside in the core-oligosaccharide of the structurally defined lipopolysaccharide (LPS), Re-LPS (Kdo2-lipid A) from Salmonella minnesota strain R595 and Escherichia coli strain D31m4, while Rd-LPS from Salmonella minnesota strain R7, that contains an extra outer core phosphorylated heptose, is only slowly hydrolyzed. The complex type LPS from Neisseria meningitides strains A1 and M992 that contain extra 5-6 sugar units at the outer core are refractory to recombinnat alpha-Kdo-ase | Crassostrea virginica | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 44604, sequence calculation | Crassostrea virginica |
Synonyms | Comment | Organism |
---|---|---|
3-deoxy-D-manno-oct-2-ulosonic acid alpha-ketoside hydrolase | - |
Crassostrea virginica |
3-deoxy-octulo-sonase | - |
Crassostrea virginica |
alpha-Kdo-ase | - |
Crassostrea virginica |
General Information | Comment | Organism |
---|---|---|
evolution | the deduced amino acid sequence of the enzyme contains two Asp boxes (S277PDDGKTW and S328TDQGKTW) commonly found in sialidases | Crassostrea virginica |